The prpE gene of Salmonella typhimurium LT2 encodes propionyl-CoA synthetase

Horswill, Alexander R.; Escalante‐Semerena, Jorge C.

doi:10.1099/13500872-145-6-1381

Cited by 80 publications

(117 citation statements)

References 34 publications

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“…Since growth on low concentrations of acetate depends on AMP-ACS while growth on high concentrations requires the PTA-ACKA pathway, mutants that lack both cannot grow on acetate at any concentration (251). The inability to grow on acetate at any concentration argues against compensation by other acetate-activating enzymes, such as propionyl-CoA synthetase, encoded by prpE (201), or the propionate kinases, encoded by tdcD in E. coli or Salmonella enterica (186) or by pduW in S. enterica (52,331). PrpE can use acetate as an alternative substrate (201); thus, PrpE can restore growth on acetate to acs pta ackA mutants, but only when expressed from a high-copy-number plasmid and then only poorly (S. Kumari and A. J. Wolfe, unpublished data).…”

Section: Acetate Activation Pathwaysmentioning

confidence: 99%

The Acetate Switch

Wolfe

2005

Microbiol Mol Biol Rev

1,066

1,274

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To succeed, many cells must alternate between life-styles that permit rapid growth in the presence of abundant nutrients and ones that enhance survival in the absence of those nutrients. One such change in life-style, the “acetate switch,” occurs as cells deplete their environment of acetate-producing carbon sources and begin to rely on their ability to scavenge for acetate. This review explains why, when, and how cells excrete or dissimilate acetate. The central components of the “switch” (phosphotransacetylase [PTA], acetate kinase [ACK], and AMP-forming acetyl coenzyme A synthetase [AMP-ACS]) and the behavior of cells that lack these components are introduced. Acetyl phosphate (acetyl∼P), the high-energy intermediate of acetate dissimilation, is discussed, and conditions that influence its intracellular concentration are described. Evidence is provided that acetyl∼P influences cellular processes from organelle biogenesis to cell cycle regulation and from biofilm development to pathogenesis. The merits of each mechanism proposed to explain the interaction of acetyl∼P with two-component signal transduction pathways are addressed. A short list of enzymes that generate acetyl∼P by PTA-ACKA-independent mechanisms is introduced and discussed briefly. Attention is then directed to the mechanisms used by cells to “flip the switch,” the induction and activation of the acetate-scavenging AMP-ACS. First, evidence is presented that nucleoid proteins orchestrate a progression of distinct nucleoprotein complexes to ensure proper transcription of its gene. Next, the way in which cells regulate AMP-ACS activity through reversible acetylation is described. Finally, the “acetate switch” as it exists in selected eubacteria, archaea, and eukaryotes, including humans, is described

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Section: Acetate Activation Pathwaysmentioning

confidence: 99%

The Acetate Switch

Wolfe

2005

Microbiol Mol Biol Rev

1,066

1,274

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“…PrpE encodes propionyl-CoA synthase. In S. enterica, acetyl-CoA synthase can substitute for PrpE, so prpE only becomes essential for growth on propionate in an acs mutant background [8]. In contrast, PrpF plays an altogether more interesting role.…”

Section: The Methylcitrate Cyclementioning

confidence: 99%

Loving the poison: the methylcitrate cycle and bacterial pathogenesis

et al. 2018

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Propionate is an abundant catabolite in nature and represents a rich potential source of carbon for the organisms that can utilize it. However, propionate and propionate-derived catabolites are also toxic to cells, so propionate catabolism can alternatively be viewed as a detoxification mechanism. In this review, we summarize recent progress made in understanding how prokaryotes catabolize propionic acid, how these pathways are regulated and how they might be exploited to develop novel antibacterial interventions.

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“…The prpE gene was amplified from plasmid pPRP68 (35), adding 5Ј-NheI and 3Ј-EcoRI sites, and ligated into plasmid pTYB12 (Novagen) cut with SpeI and EcoRI. The resulting plasmid, pPRP211, was used to produce PrpE with an N-terminal chitin-binding domain in strains JE9221 (⌬acs ⌬cobB/pTARA rpo ϩ /pPRP211 prpE ϩ ) and JE9225 (⌬acs ⌬cobB pat/pTARA T7 rpo ϩ /pPRP211 prpE ϩ ).…”

Section: In Vivo Modification Of Prpementioning

confidence: 99%

N-Lysine Propionylation Controls the Activity of Propionyl-CoA Synthetase

Garrity

Gardner

Hawse

et al. 2007

Journal of Biological Chemistry

Self Cite

183

229

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Reversible protein acetylation is a ubiquitous means for the rapid control of diverse cellular processes. Acetyltransferase enzymes transfer the acetyl group from acetyl-CoA to lysine residues, while deacetylase enzymes catalyze removal of the acetyl group by hydrolysis or by an NAD ؉ -dependent reaction. Propionyl-coenzyme A (CoA), like acetyl-CoA, is a high energy product of fatty acid metabolism and is produced through a similar chemical reaction. Because acetyl-CoA is the donor molecule for protein acetylation, we investigated whether proteins can be propionylated in vivo, using propionyl-CoA as the donor molecule. We report that the Salmonella enterica propionyl-CoA synthetase enzyme PrpE is propionylated in vivo at lysine 592; propionylation inactivates PrpE. The propionyl-lysine modification is introduced by bacterial Gcn-5-related N-acetyltransferase enzymes and can be removed by bacterial and human Sir2 enzymes (sirtuins). Like the sirtuin deacetylation reaction, sirtuin-catalyzed depropionylation is NAD ؉ -dependent and produces a byproduct, O-propionyl ADP-ribose, analogous to the O-acetyl ADP-ribose sirtuin product of deacetylation. Only a subset of the human sirtuins with deacetylase activity could also depropionylate substrate. The regulation of cellular propionylCoA by propionylation of PrpE parallels regulation of acetylCoA by acetylation of acetyl-CoA synthetase and raises the possibility that propionylation may serve as a regulatory modification in higher organisms.Protein acetylation is a ubiquitous means for the rapid control of diverse cellular processes (1, 2). Acetylation occurs at lysine residues, with acetyl-CoA (Ac-CoA) 5 serving as the acetyl group donor. In higher organisms, aberrant acetylation of lysine residues in histone tails correlates with diseases such as cancers and developmental disorders and may contribute to modulation of cell life span (3, 4). From bacteria to humans, N-Lys acetylation controls the activity of acetyl-coenzyme A synthetase (AMP-forming; Acs) and potentially that of other members of the AMP-forming family of enzymes (5-7). In Salmonella enterica, Acs is deacetylated by CobB, a member of the Sir2 family of NAD ϩ -dependent deacetylases (a.k.a. sirtuins) (8). Interestingly, strains of S. enterica lacking CobB deacetylase activity cannot grow on propionate because the propionyl-CoA synthetase (encoded by the prpE gene) that activates propionate to propionyl-CoA is not active (5, 9).Cells generate propionyl-CoA from several different processes, including the catabolism of odd chain fatty acids, the decarboxylation of succinate, the catabolism of amino acids (e.g. threonine), and the activation of propionate (10 -12). Propionate is a powerful inhibitor of cell growth that is widely used as a food preservative. Reports in the literature suggest that propionyl-CoA may be responsible for the cytotoxic effects of propionate. Although the direct effects of propionyl-CoA are unclear, it is clear that cells avoid accumulating this metabolite (13-15). The cell maintains...

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The prpE gene of Salmonella typhimurium LT2 encodes propionyl-CoA synthetase

Cited by 80 publications

References 34 publications

The Acetate Switch

The Acetate Switch

Loving the poison: the methylcitrate cycle and bacterial pathogenesis

N-Lysine Propionylation Controls the Activity of Propionyl-CoA Synthetase

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